Piehl Michelle, Tulu U Serdar, Wadsworth Pat, Cassimeris Lynne
Department of Biological Sciences, Lehigh University, 111 Research Drive, Bethlehem, PA 18015, USA.
Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1584-8. doi: 10.1073/pnas.0308205100. Epub 2004 Jan 27.
Understanding how cells regulate microtubule nucleation during the cell cycle has been limited by the inability to directly observe nucleation from the centrosome. To view nucleation in living cells, we imaged GFP-tagged EB1, a microtubule tip-binding protein, and determined rates of nucleation by counting the number of EB1-GFP comets emerging from the centrosome over time. Nucleation rate increased 4-fold between G(2) and prophase and continued to rise through anaphase and telophase, reaching a maximum of 7 times interphase rates. We tested several models for centrosome maturation, including gamma-tubulin recruitment and increased centrosome size. The centrosomal concentration of gamma-tubulin reached a maximum at metaphase, and centrosome size increased through anaphase, whereas nucleation remained high through telophase, implying the presence of additional regulatory processes. Injection of anti-gamma-tubulin antibodies significantly blocked nucleation during metaphase but was less effective during anaphase, suggesting that a nucleation mechanism independent of gamma-tubulin contributes to centrosome function after metaphase.
由于无法直接观察中心体的微管成核过程,了解细胞在细胞周期中如何调节微管成核一直受到限制。为了观察活细胞中的成核过程,我们对绿色荧光蛋白标记的EB1(一种微管末端结合蛋白)进行成像,并通过计算随着时间推移从中心体出现的EB1-绿色荧光蛋白彗星的数量来确定成核速率。在G2期和前期之间,成核速率增加了4倍,并在后期和末期持续上升,最高达到间期速率的7倍。我们测试了几种中心体成熟模型,包括γ-微管蛋白的募集和中心体大小的增加。γ-微管蛋白的中心体浓度在中期达到最大值,中心体大小在后期增加,而成核在末期仍然很高,这意味着存在其他调节过程。注射抗γ-微管蛋白抗体在中期显著阻断了成核,但在后期效果较差,这表明在中期之后,一种独立于γ-微管蛋白的成核机制对中心体功能有贡献。